| Structural highlights
Function
[VP16_BPPRD] protein of the infection vertex complex, which increases the vertex stability. Anchors the vertex structure to the viral membrane. Essential for viral infectivity.[1] [CAPSD_BPPRD] Major capsid protein self-assembles to form an icosahedral capsid with a pseudo T=25 symmetry, about 66 nm in diameter, and consisting of 240 capsid proteins trimers. The capsid encapsulates an inner membrane and the genomic dsDNA genome. The major coat protein P3 and two assembly factors (P10 and P17) are needed during the assembly of the virus particle inside the host cell, when the capsid protein multimers are capable of enclosing the host-derived membrane, containing the virus-encoded membrane-associated proteins. [VP31_BPPRD] In association with P2 and trimeric P5, forms the spike complexes located at the 5-fold vertices of the capsid. Essential for viral infectivity. [VP30_BPPRD] Minor capsid protein essential for stable capsid assembly of complete particles.[2]
Publication Abstract from PubMed
The structure of the membrane-containing bacteriophage PRD1 has been determined by X-ray crystallography at about 4 A resolution. Here we describe the structure and location of proteins P3, P16, P30 and P31. Different structural proteins seem to have specialist roles in controlling virus assembly. The linearly extended P30 appears to nucleate the formation of the icosahedral facets (composed of trimers of the major capsid protein, P3) and acts as a molecular tape-measure, defining the size of the virus and cementing the facets together. Pentamers of P31 form the vertex base, interlocking with subunits of P3 and interacting with the membrane protein P16. The architectural similarities with adenovirus and one of the largest known virus particles PBCV-1 support the notion that the mechanism of assembly of PRD1 is scaleable and applies across the major viral lineage formed by these viruses.
Insights into assembly from structural analysis of bacteriophage PRD1.,Abrescia NG, Cockburn JJ, Grimes JM, Sutton GC, Diprose JM, Butcher SJ, Fuller SD, San Martin C, Burnett RM, Stuart DI, Bamford DH, Bamford JK Nature. 2004 Nov 4;432(7013):68-74. PMID:15525981[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jaatinen ST, Viitanen SJ, Bamford DH, Bamford JK. Integral membrane protein P16 of bacteriophage PRD1 stabilizes the adsorption vertex structure. J Virol. 2004 Sep;78(18):9790-7. PMID:15331712 doi:http://dx.doi.org/10.1128/JVI.78.18.9790-9797.2004
- ↑ Rydman PS, Bamford JK, Bamford DH. A minor capsid protein P30 is essential for bacteriophage PRD1 capsid assembly. J Mol Biol. 2001 Nov 2;313(4):785-95. PMID:11697904 doi:http://dx.doi.org/10.1006/jmbi.2001.5068
- ↑ Abrescia NG, Cockburn JJ, Grimes JM, Sutton GC, Diprose JM, Butcher SJ, Fuller SD, San Martin C, Burnett RM, Stuart DI, Bamford DH, Bamford JK. Insights into assembly from structural analysis of bacteriophage PRD1. Nature. 2004 Nov 4;432(7013):68-74. PMID:15525981 doi:10.1038/nature03056
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